ID   BIOC_PSEVU              Reviewed;         251 AA.
AC   O06898;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Malonyl-[acyl-carrier protein] O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE            Short=Malonyl-ACP O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00835};
DE            EC=2.1.1.197 {ECO:0000255|HAMAP-Rule:MF_00835};
DE   AltName: Full=Biotin synthesis protein BioC {ECO:0000255|HAMAP-Rule:MF_00835};
GN   Name=bioC {ECO:0000255|HAMAP-Rule:MF_00835};
OS   Pseudescherichia vulneris (Escherichia vulneris).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pseudescherichia.
OX   NCBI_TaxID=566;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 39368 / Eho10;
RX   PubMed=9063571; DOI=10.1080/15216549700201321;
RA   Wu C.H., Bao Y.Y., Shao C.P., Shiuan D.;
RT   "Molecular cloning and nucleotide sequencing of bioF (7-keto-8-amino
RT   pelargonic acid synthetase), bioC and bioD (dethiobiotin synthetase) genes
RT   of Erwinia herbicola.";
RL   Biochem. Mol. Biol. Int. 41:311-315(1997).
CC   -!- FUNCTION: Converts the free carboxyl group of a malonyl-thioester to
CC       its methyl ester by transfer of a methyl group from S-adenosyl-L-
CC       methionine (SAM). It allows to synthesize pimeloyl-ACP via the fatty
CC       acid synthetic pathway. {ECO:0000255|HAMAP-Rule:MF_00835}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=malonyl-[ACP] + S-adenosyl-L-methionine = malonyl-[ACP] methyl
CC         ester + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:17105, Rhea:RHEA-
CC         COMP:9623, Rhea:RHEA-COMP:9954, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789,
CC         ChEBI:CHEBI:78449, ChEBI:CHEBI:78845; EC=2.1.1.197;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00835};
CC   -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00835}.
CC   -!- SIMILARITY: Belongs to the methyltransferase superfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00835}.
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DR   EMBL; U51207; AAB52911.1; -; Genomic_DNA.
DR   AlphaFoldDB; O06898; -.
DR   UniPathway; UPA00078; -.
DR   GO; GO:0010340; F:carboxyl-O-methyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0102130; F:malonyl-CoA methyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.150; -; 1.
DR   HAMAP; MF_00835; BioC; 1.
DR   InterPro; IPR011814; BioC.
DR   InterPro; IPR013216; Methyltransf_11.
DR   InterPro; IPR029063; SAM-dependent_MTases_sf.
DR   Pfam; PF08241; Methyltransf_11; 1.
DR   SUPFAM; SSF53335; SSF53335; 1.
DR   TIGRFAMs; TIGR02072; BioC; 1.
PE   3: Inferred from homology;
KW   Biotin biosynthesis; Methyltransferase; S-adenosyl-L-methionine;
KW   Transferase.
FT   CHAIN           1..251
FT                   /note="Malonyl-[acyl-carrier protein] O-methyltransferase"
FT                   /id="PRO_0000204417"
SQ   SEQUENCE   251 AA;  27411 MW;  72517B366A87AA7A CRC64;
     MSLVNKRAVA AAFGRAAQSY DSHAQLQRQS ADLLLAKLGE RRPASVLDAG CGPGSMSRYW
     RDAGAEVTAL DLSLPMLRQA QSQQAAQHYV AADIEALPLA DARFDLAWSN LAVQWCNDLG
     QALKSLHRVV RPGGAVAFTT LASGSLPELH QAWQAVDSRL HANRFLAEET LAETVSAWRG
     QWGIEPVTLA FDDALAAMRS LKGIGATHLH AGRHNTPLTR GQLQRLQLAW PQQQGRCLLT
     YSLFWGVIER D